Woodward J R, Kornberg H L
Biochem J. 1980 Nov 15;192(2):659-64. doi: 10.1042/bj1920659.
Cells of the wild-type yeast (Saccharomyces cerevisiae) strain Y185, grown under conditions that de-repress the formation of a general amino acid permease ('Gap') system, bind delta-N-chloroacetyl[1-(14)C]ornithine; L- and D-amino acid substrates of the general amino acid permease system protect against this binding. The protein responsible is released from the cells by homogenization or by preparation of protoplasts; it is not released by osmotic shock. This protein is virtually absent from the wild-type strain when it is grown under conditions that repress the general amino acid permease system, and is also absent from a Gap- mutant Y185-His3, selected by its resistance to D-amino acids. This mutant and repressed wild-type cells also fail to form a number of membrane proteins elaborated by de-repressed wild-type cells. It is possible that all these proteins are components of the general amino acid permease system.
在能解除对一种通用氨基酸通透酶（“Gap”）系统形成抑制的条件下生长的野生型酵母（酿酒酵母）菌株Y185的细胞，能结合δ-N-氯乙酰基-[1-(14)C]鸟氨酸；通用氨基酸通透酶系统的L-和D-氨基酸底物可防止这种结合。负责此功能的蛋白质可通过匀浆或制备原生质体从细胞中释放出来；但不能通过渗透休克释放。当野生型菌株在抑制通用氨基酸通透酶系统的条件下生长时，这种蛋白质几乎不存在，并且对D-氨基酸具有抗性的Gap-突变体Y185-His3中也不存在。这种突变体和受抑制的野生型细胞也无法形成一些由解除抑制的野生型细胞所合成的膜蛋白。所有这些蛋白质有可能都是通用氨基酸通透酶系统的组成成分。
